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Related Experiment Videos

Methionine residue accessibility in native subtilisin DY.

A Lilova, T Kleinschmidt, P Nedkov

    Biological Chemistry Hoppe-Seyler
    |May 1, 1987
    PubMed
    Summary

    Subtilisin DY

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Protein Chemistry

    Background:

    • Subtilisin DY contains three methionine residues.
    • Understanding methionine residue exposure is crucial for enzyme function.
    • Oxidation can alter enzyme activity and structure.

    Purpose of the Study:

    • To determine the accessibility of methionine residues in subtilisin DY.
    • To investigate the impact of methionine oxidation on subtilisin DY activity.

    Main Methods:

    • Chemical modification of methionine residues using chloramine T.
    • Peptide mapping via cyanogen bromide treatment, gel chromatography, and Edman degradation.
    • Structural analysis using a computer graphics model of subtilisin Carlsberg.

    Main Results:

    • Met222 is surface-exposed, Met124 is partially exposed, and Met199 is buried.
    • Oxidation of surface-exposed Met222 (adjacent to Ser221) caused a 25% loss in caseinolytic activity.
    • Each additional methionine modification resulted in a 5% activity decrease.

    Conclusions:

    • Methionine residue accessibility correlates with structural location.
    • Oxidation of methionine residues, particularly those near the active site, significantly impairs subtilisin DY activity.
    • Specific methionine modifications provide insights into enzyme stability and function.

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